Extracellular matrix metalloproteinase (MMP) inducer (EMMPRIN), also known as basigin and CD147, is a 44 66 kDa, variably N and O glycosylated, type I transmembrane protein that belongs to the immunoglobulin superfamily. Human EMMPRIN is 269 amino acids (aa) in length and contains a 24 aa signal sequence, a 183 aa extracellular domain (ECD), a 21 aa transmembrane (TM) segment and a 41 aa cytoplasmic tail. The ECD contains one C2 type and one V type Ig like domain. EMMPRIN is expressed in areas of tissue remodeling, including endometrium, placenta, skin, and regions undergoing angiogenesis. It is also expressed on cells with high metabolic activity, such as lymphoblasts, macrophages and particularly tumor cells. A functional ELISA assay was conducted to detect the interaction of recombinant Human EMMPRIN/CD147 and recombinant rat Cyclophilin B (CYPB) . Briefly, biotin-linked CD147 were diluted serially in PBS, with 0.01% BSA (pH 7.4). Duplicate samples of 100 μl were then transferred to CYPB-coated microtiter wells and incubated for 1h at 37℃. Wells were washed with PBST 3 times and incubation with Streptavidin-HRP for 30min, then wells were aspirated and washed 5 times. With the addition of substrate solution, wells were incubated 15-25 minutes at 37℃. Finally, add 50 μl stop solution to the wells and read at 450 nm immediately. The binding activity of CD147 and CYPB was shown in Figure 1, the EC50 for this effect is 53.34 ug/mL.